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. 1982 Nov 1;207(2):357–362. doi: 10.1042/bj2070357

Steady-state kinetic studies of the inhibitory action of Zn2+ on ribonuclease T1 catalysis.

M Itaya, Y Inoue
PMCID: PMC1153868  PMID: 6818948

Abstract

The kinetic mechanism of specific inhibition by Zn2+ of ribonuclease T1 catalysis was studied by steady-state kinetic analysis of transphosphorylation of dinucleotides, GpCp(3'), GpUp(2') and GpUp(3'), and dinucleoside monophosphates, GpC and GpU. The inhibition was not simply competitive, non-competitive or uncompetitive, but the kinetic data were compatible with a mechanism of 'fully mixed inhibition' in which a fully non-competitive action was associated with a partially competitive action. Apparent equilibrium quotients involved in this model of inhibition were determined for the dinucleotide substrates, and we found that binding of either of Zn2+ and substrate was facilitated when the other was bound. The location of Zn2+ was suggested to be near His-40 and/or His-92 of the ribonuclease T1 molecule.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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